Meta-Biol

• Pathways

FGFR2 S267P undergoes ligand-independent dimerization, and appears unable to stably bind FGF2 ligand under the conditions examined (Anderson, 1998). FGFR2b S373C and Y376C are paralogous to the FGFR3 S371C and Y373C mutations that are seen in thanatophoric dysplasia I (Rousseau, 1996; Tavormina, 1995a) and which have been shown to undergo spontaneous dimerization in the absence of ligand (d'Avis, 1998; Adar, 2002). Moreover, other FGFR2 mutations that introduce unpaired cysteine residues have been shown to support formation of intermolecular disulphide bonds (Galvin, 1996; Neilson and Friesel, 1995), supporting the notion that the FGFR2b S373C and Y376C mutants may promote spontaneous receptor dimerization and activation.